LCF3_YEAST
ID LCF3_YEAST Reviewed; 694 AA.
AC P39002; D6VVS1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Long-chain-fatty-acid--CoA ligase 3;
DE EC=6.2.1.3 {ECO:0000269|PubMed:8206942};
DE AltName: Full=Fatty acid activator 3;
DE AltName: Full=Long-chain acyl-CoA synthetase 3;
GN Name=FAA3; OrderedLocusNames=YIL009W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8027063; DOI=10.1016/s0021-9258(17)32414-6;
RA Johnson D.R., Knoll L.J., Rowley N., Gordon J.I.;
RT "Genetic analysis of the role of Saccharomyces cerevisiae acyl-CoA
RT synthetase genes in regulating protein N-myristoylation.";
RL J. Biol. Chem. 269:18037-18046(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8206942; DOI=10.1016/s0021-9258(17)34014-0;
RA Knoll L.J., Johnson D.R., Gordon J.I.;
RT "Biochemical studies of three Saccharomyces cerevisiae acyl-CoA
RT synthetases, Faa1p, Faa2p, and Faa3p.";
RL J. Biol. Chem. 269:16348-16356(1994).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH FRK1.
RX PubMed=20489023; DOI=10.1126/science.1176495;
RA Breitkreutz A., Choi H., Sharom J.R., Boucher L., Neduva V., Larsen B.,
RA Lin Z.Y., Breitkreutz B.J., Stark C., Liu G., Ahn J., Dewar-Darch D.,
RA Reguly T., Tang X., Almeida R., Qin Z.S., Pawson T., Gingras A.C.,
RA Nesvizhskii A.I., Tyers M.;
RT "A global protein kinase and phosphatase interaction network in yeast.";
RL Science 328:1043-1046(2010).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Activates endogenous long-chain fatty acids (LCFA) by
CC esterification of the fatty acids into metabolically active CoA-
CC thioesters for subsequent degradation or incorporation into
CC phospholipids (PubMed:8206942). Acts preferentially on C16 and C18
CC fatty acids with a cis-double bond at C-9-C-10 (PubMed:8206942).
CC {ECO:0000269|PubMed:8206942}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-
CC CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560,
CC ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3;
CC Evidence={ECO:0000269|PubMed:8206942};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate + ATP + CoA = (9Z)-octadecenoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:33607, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:8206942};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33608;
CC Evidence={ECO:0000305|PubMed:8206942};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + hexadecanoate = AMP + diphosphate + hexadecanoyl-
CC CoA; Xref=Rhea:RHEA:30751, ChEBI:CHEBI:7896, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:8206942};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
CC Evidence={ECO:0000305|PubMed:8206942};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoate + ATP + CoA = (9Z)-hexadecenoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:33647, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:32372, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:61540, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:8206942};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33648;
CC Evidence={ECO:0000305|PubMed:8206942};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-tetradecenoate + ATP + CoA = (9Z)-tetradecenoyl-CoA + AMP
CC + diphosphate; Xref=Rhea:RHEA:33643, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:32370, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:65060, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:8206942};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33644;
CC Evidence={ECO:0000305|PubMed:8206942};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + ATP + CoA = (9Z,12Z)-
CC octadecadienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:33651,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:8206942};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33652;
CC Evidence={ECO:0000305|PubMed:8206942};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P30624};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.7. {ECO:0000269|PubMed:8206942};
CC Temperature dependence:
CC Optimum temperature is 25 degrees Celsius.
CC {ECO:0000269|PubMed:8206942};
CC -!- SUBUNIT: Interacts with FRK1. {ECO:0000269|PubMed:20489023}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: The FACS motif is required for catalytic activity and substrate
CC specificity. {ECO:0000250|UniProtKB:P30624}.
CC -!- MISCELLANEOUS: Present with 6440 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z29647; CAA82755.1; -; Genomic_DNA.
DR EMBL; Z38113; CAA86241.1; -; Genomic_DNA.
DR EMBL; AY558110; AAS56436.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08537.1; -; Genomic_DNA.
DR PIR; B54901; B54901.
DR RefSeq; NP_012257.1; NM_001179359.1.
DR AlphaFoldDB; P39002; -.
DR SMR; P39002; -.
DR BioGRID; 34983; 52.
DR DIP; DIP-4210N; -.
DR IntAct; P39002; 8.
DR MINT; P39002; -.
DR STRING; 4932.YIL009W; -.
DR SwissLipids; SLP:000001033; -.
DR iPTMnet; P39002; -.
DR MaxQB; P39002; -.
DR PaxDb; P39002; -.
DR PRIDE; P39002; -.
DR EnsemblFungi; YIL009W_mRNA; YIL009W; YIL009W.
DR GeneID; 854808; -.
DR KEGG; sce:YIL009W; -.
DR SGD; S000001271; FAA3.
DR VEuPathDB; FungiDB:YIL009W; -.
DR eggNOG; KOG1180; Eukaryota.
DR GeneTree; ENSGT00940000171609; -.
DR HOGENOM; CLU_000022_45_2_1; -.
DR InParanoid; P39002; -.
DR OMA; WEWLASI; -.
DR BioCyc; YEAST:YIL009W-MON; -.
DR Reactome; R-SCE-434313; Intracellular metabolism of fatty acids regulates insulin secretion.
DR Reactome; R-SCE-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR PRO; PR:P39002; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P39002; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005811; C:lipid droplet; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:SGD.
DR GO; GO:0031957; F:very long-chain fatty acid-CoA ligase activity; IDA:SGD.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; IGI:SGD.
DR GO; GO:0035336; P:long-chain fatty-acyl-CoA metabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cell membrane; Fatty acid metabolism; Ligase;
KW Lipid metabolism; Magnesium; Membrane; Nucleotide-binding;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..694
FT /note="Long-chain-fatty-acid--CoA ligase 3"
FT /id="PRO_0000193121"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 527..576
FT /note="FACS"
FT /evidence="ECO:0000250|UniProtKB:P30624"
FT BINDING 269..280
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69451"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 694 AA; 77947 MW; 7AB33044335A5295 CRC64;
MSEQHSVAVG KAANEHETAP RRNVRVKKRP LIRPLNSSAS TLYEFALECF NKGGKRDGMA
WRDVIEIHET KKTIVRKVDG KDKSIEKTWL YYEMSPYKMM TYQELIWVMH DMGRGLAKIG
IKPNGEHKFH IFASTSHKWM KIFLGCISQG IPVVTAYDTL GESGLIHSMV ETESAAIFTD
NQLLAKMIVP LQSAKDIKFL IHNEPIDPND RRQNGKLYKA AKDAINKIRE VRPDIKIYSF
EEVVKIGKKS KDEVKLHPPE PKDLACIMYT SGSISAPKGV VLTHYNIVSG IAGVGHNVFG
WIGSTDRVLS FLPLAHIFEL VFEFEAFYWN GILGYGSVKT LTNTSTRNCK GDLVEFKPTI
MIGVAAVWET VRKAILEKIS DLTPVLQKIF WSAYSMKEKS VPCTGFLSRM VFKKVRQATG
GHLKYIMNGG SAISIDAQKF FSIVLCPMII GYGLTETVAN ACVLEPDHFE YGIVGDLVGS
VTAKLVDVKD LGYYAKNNQG ELLLKGAPVC SEYYKNPIET AVSFTYDGWF RTGDIVEWTP
KGQLKIIDRR KNLVKTLNGE YIALEKLESV YRSNSYVKNI CVYADESRVK PVGIVVPNPG
PLSKFAVKLR IMKKGEDIEN YIHDKALRNA VFKEMIATAK SQGLVGIELL CGIVFFDEEW
TPENGFVTSA QKLKRREILA AVKSEVERVY KENS
